# Structure of importin-β bound to the IBB domain of importin-α

@article{Cingolani1999StructureOI,
title={Structure of importin-$\beta$ bound to the IBB domain of importin-$\alpha$},
author={Gino Cingolani and Carlo Petosa and Karsten Weis and Christoph W. M{\"u}ller},
journal={Nature},
year={1999},
volume={399},
pages={221-229}
}
• Published 20 May 1999
• Chemistry, Biology
• Nature
Cytosolic proteins bearing a classical nuclear localization signal enter the nucleus bound to a heterodimer of importin-α and importin-β (also called karyopherin-α and -β). The formation of this heterodimer involves the importin-β-binding (IBB) domain of importin-α, a highly basic amino-terminal region of roughly 40 amino-acid residues. Here we report the crystal structure of human importin-β bound to the IBB domain of importin-α, determined at 2.5 Å and 2.3 Å resolution in two crystal forms…
379 Citations
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• 2001
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Biochemical propensity mapping for structural and functional anatomy of importin α IBB domain
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This study distinguished the location and properties of amino acids important for each function of the importin α I BB domain by mapping the biochemical/physicochemical propensities of evolutionarily conserved amino acids of the IBB domain onto the structure associated with each function.
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This study distinguished the location and propensities of amino acids important for each function of the importin α IBB domain by mapping the biochemical/physicochemical propensity of evolutionarily conserved amino acids of the I BB domain onto the structure associated with each function.
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